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Lookup NU author(s): Dr Claire Townes, Panagiota Milona, Dr Judith HallORCiD
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AWAP IV constitutes the C-terminal domain of the larger 81 kDa protein AWAK [Avian WAP (whey acidic protein) domain- and Kunitz domain-containing], which is predicted, through conserved domain database searching, to contain at least four WAP domains and one Kunitz domain. RT (reverse transcription)-PCR analyses revealed mRNA transcripts encoding AWAP IV in the small intestinal and kidney tissues of 5-day-old Salmonella-infected chicks. Time-kill antimicrobial assays using rAWAP IV (recombinant AWAP IV) cell lysate indicated antimicrobial activity against Gram-positive and Gram-negative bacteria including Salmonella, Streptococcus and Staphylococcus spp. In addition, permeabilization of the outer membrane of Salmonella, as shown by the NPN (N-phenyl-1-naphthylamine) fluorescent probe assay, supported the ability of rAWAP IV to disrupt prokaryotic membranes. WAP domains can function as inhibitors of serine protease activity, and the microbial serine proteases subtilisin and proteinase K were inhibited by rAWAP IV cell lysate. However, at comparable concentrations, no significant inhibition of the mammalian serine protease elastase was observed. The combined broad-spectrum antibacterial and anti-protease activities of AWAP IV suggest a novel role in the avian innate defence mechanisms operating against microbial infection. ©2006 Biochemical Society.
Author(s): Townes CL, Milona P, Hall J
Publication type: Conference Proceedings (inc. Abstract)
Publication status: Published
Conference Name: Conference on Antimicrobial Peptides - Mediators of Innate Immunity in the Development of Anti-Infective, Therapeutic and Vaccination Strategies
Year of Conference: 2006
Pages: 267-269
ISSN: 0300-5127
Publisher: Biochemical Society Transactions, Portland Press Ltd.
URL: http://dx.doi.org/10.1042/BST20060267
DOI: 10.1042/BST20060267
PubMed id: 16545090
Library holdings: Search Newcastle University Library for this item
ISBN: 14708752
